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Database: UniProt
Entry: A5F331
LinkDB: A5F331
Original site: A5F331 
ID   DXS_VIBC3               Reviewed;         626 AA.
AC   A5F331; C3LYQ3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   01-OCT-2014, entry version 52.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315};
GN   OrderedLocusNames=VC0395_A0412, VC395_0905;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y.,
RA   Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the
RT   cholera pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC       atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC       1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC       5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR   EMBL; CP000627; ABQ21549.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08919.1; -; Genomic_DNA.
DR   RefSeq; YP_001216367.1; NC_009457.1.
DR   RefSeq; YP_002819155.1; NC_012582.1.
DR   ProteinModelPortal; A5F331; -.
DR   SMR; A5F331; 3-625.
DR   STRING; 345073.VC0395_A0412; -.
DR   EnsemblBacteria; ABQ21549; ABQ21549; VC0395_A0412.
DR   EnsemblBacteria; ACP08919; ACP08919; VC395_0905.
DR   GeneID; 5136254; -.
DR   GeneID; 7774897; -.
DR   KEGG; vco:VC0395_A0412; -.
DR   KEGG; vcr:VC395_0905; -.
DR   eggNOG; COG1154; -.
DR   HOGENOM; HOG000012988; -.
DR   KO; K01662; -.
DR   OMA; MSTIRQK; -.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 3.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    626       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_1000071998.
FT   REGION      121    123       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      153    154       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       152    152       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       181    181       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      80     80       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     181    181       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     288    288       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     370    370       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   626 AA;  68347 MW;  5E83BF99EE8C51C9 CRC64;
     MTLDISKYPT LALANTPDEL RSLPKEVLPK LCDELRTYLL NSVSQSSGHL ASGLGTVELT
     VALHYVYHTP FDHLIWDVGH QAYPHKILTG RRDQMPTIRQ KDGLHPFPWR EESEYDTLSV
     GHSSTSISAA LGMAICAGKE GKDRKVVSVI GDGAITAGMA FEAMNHAGDV HPDMLVVLND
     NEMSISENVG ALNNHLAQVL SGSLYTSIRE GGKKVLSGIP PIKELVRRTE EHLKGMVVPG
     TLFEELGFNY IGPVDGHDVL ELIKTLKNMR ELKGPQFLHV MTKKGKGYAP AEKDPIGYHG
     VPKFDPSHHS LPKSSNTKPT FSKIFGDFLC DMAAQDPKLM AITPAMREGS GMVRFSKEYP
     SQYFDVAIAE QHAVTLATGM AIAGYHPIVA IYSTFLQRGY DQLIHDVAIM NLPVMFAIDR
     AGIVGADGQT HQGAFDLSYM RCIPNMLIMA PADENECRQM LYTGHQHQGP SAVRYPRGNG
     MGVELESSFT ALEIGKGRLM RESTACEGEK VAILSFGTLL PNALQAAEKL NATVADMRFV
     KPLDEALIKQ LAQTHDVLVT LEENAIAGGA GAGVIEFLMK EKQLKPVLNL GLPDQFIVQG
     TQEEMHAELG LDGAGIERAI RDYLAK
//
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